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Database: UniProt
Entry: R7IBI1_9FIRM
LinkDB: R7IBI1_9FIRM
Original site: R7IBI1_9FIRM 
ID   R7IBI1_9FIRM            Unreviewed;       818 AA.
AC   R7IBI1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN   ORFNames=BN770_01950 {ECO:0000313|EMBL:CDE49234.1};
OS   Faecalibacterium sp. CAG:74.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=1262897 {ECO:0000313|EMBL:CDE49234.1, ECO:0000313|Proteomes:UP000018328};
RN   [1] {ECO:0000313|EMBL:CDE49234.1, ECO:0000313|Proteomes:UP000018328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:74 {ECO:0000313|Proteomes:UP000018328};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC         in beta-D-mannosides.; EC=3.2.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000829};
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000256|ARBA:ARBA00004740}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE49234.1}.
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DR   EMBL; CBJB010000139; CDE49234.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7IBI1; -.
DR   Proteomes; UP000018328; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR041625; Beta-mannosidase_Ig.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018328};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          187..274
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          661..745
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          749..815
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   818 AA;  93765 MW;  2C6F9F64D9E0AF07 CRC64;
     MTEQVNLGGA WRMREADSET WHSAHVPGSV YADLTADGTM PDPFWRENEL DAFERMKKDY
     VYQRAFTVTE AQLAHAHVEL VCEGLDTLAH VSLNGREIAF ADNMHITWVW DVKEQLHAGE
     NTLEIRFDSP ILYCAKKAEE APGWESSDAT PGFRHLRKAH CMFGWDWGPR LPDAGIWRPI
     FLRTWDTARL ENALMLQAHH DGVVDVTIRP EIAGESAWSA EITAPDGEVL TLPETMAAEQ
     VIAIQNPQLW WPNGLGKQPL YRVTVRLATG DTRMWRIGLR TMTVSREKDE WGEEFCHVVN
     GMKVFAMGAD YIPEDNILAR VTPERTRRLL EDCKAANFNA IRVWGGGYYP DDAFYDICDE
     LGLLVWQDLM YACAFYDLTP DFERSIRVET HQNVARLRHH ASLALICGNN EMEMFMAGAN
     SALINHRTWE FVPTYPHHIT DYVKMFEYIL PAIVKETAPQ TYWWPASPSS GGNFDAPNDE
     NRGDNHYWDV WHGEKPFTEY RKFFFRYASE FGFQSFPCLK SVKQFTLPDD RNIFSRVMER
     HQRNQAANGK ILSYLSQTFR YPNSFDDLLY ASQLMQAEAI RYGVEHWRRN RGRCMGAIIW
     QLNDIWPVAS WASIDYYGRW KALHYAAKRF FAPVMISAEE EGELSQNPKI NEYHPAPLEK
     SFRLNVCNET LRDVTGEVVW ALRTPDGAIV RQNQQTLTIP AMSAKWLDKV DCADASLTGH
     YVSFAFVVDD VALSEGTCIF CAPKHFEFVD PRLTLETRGD TLVVTSHAYA KQVWLESEDA
     DLLLDDNAFD MNPGTKVVRV VQGSAEKVRG RSVWDLGR
//
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